ID A0A0N1ILV0_LEPSE Unreviewed; 516 AA.
AC A0A0N1ILV0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ABL78_1999 {ECO:0000313|EMBL:KPI88882.1};
OS Leptomonas seymouri.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI88882.1, ECO:0000313|Proteomes:UP000038009};
RN [1] {ECO:0000313|EMBL:KPI88882.1, ECO:0000313|Proteomes:UP000038009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI88882.1,
RC ECO:0000313|Proteomes:UP000038009};
RX PubMed=26317207;
RA Kraeva N., Butenko A., Hlavacova J., Kostygov A., Myskova J., Grybchuk D.,
RA Lestinova T., Votypka J., Volf P., Opperdoes F., Flegontov P., Lukes J.,
RA Yurchenko V.;
RT "Leptomonas seymouri: Adaptations to the Dixenous Life Cycle Analyzed by
RT Genome Sequencing, Transcriptome Profiling and Co-infection with Leishmania
RT donovani.";
RL PLoS Pathog. 11:E1005127-E1005127(2015).
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPI88882.1}.
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DR EMBL; LJSK01000037; KPI88882.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1ILV0; -.
DR EnsemblProtists; KPI88882; KPI88882; ABL78_1999.
DR VEuPathDB; TriTrypDB:Lsey_0037_0130; -.
DR OMA; ELTMDYR; -.
DR OrthoDB; 167616at2759; -.
DR Proteomes; UP000038009; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd20071; SET_SMYD; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR011095; Dala_Dala_lig_C.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR PANTHER; PTHR23132:SF28; PROTEIN WITH D-ALANINE--D-ALANINE LIGASE C-TERMINAL DOMAIN; 1.
DR Pfam; PF07478; Dala_Dala_lig_C; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50280; SET; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 119..337
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 344..461
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
SQ SEQUENCE 516 AA; 59175 MW; 90D995986287FF86 CRC64;
MSKPALKRIR VCVLACSYEG SDSELKEYEG DIVQTPQNFF DPDDPHYTFH LELIKKATAY
RQIRQLVMSG NYDVFYNQCD GAKDEDRAGV EVVEALEEFK APYTGAISKY YEMSKPDMKL
VAHYYEIATA KYAVLESGDD IPALCAHLRF PCIIKHISGY SSVGMDKSCK VYNMKELEWR
AIRFMREYQF ALIEEFISGD EATILACNDA SQPEGVRVFP PVQVTFPEGE DFKHFQLKWA
SYEGMEWTQV PESDPAMADM VSIARSAFKR MMGGIGYGRI DVRIDREHGN KVIFLEINPN
CGIMYPYGQE GSADWILRLN KGFQQRDFAK LQIHEAMERC RRERPLYIRR FDPVRGYHLR
ASEDISNGTI VFCDECRPVR LCTRPYVEDH FSKVDYEDFR HNAWPIGRSG HYYALWDRSP
SHWRAFNHSC EPNMAFAPHH SLNVVALRNI PKGEELTMDY RQFMDSTMPG FVCNCNSDKC
EGFVTPGSLA SSPVAMVAAK PPMLLHANQL LQLNPA
//
